ID   E1104_IXORI             Reviewed;          94 AA.
AC   A0A090XA85;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   26-NOV-2014, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Evasin P1104 {ECO:0000303|PubMed:31167786};
DE   Flags: Precursor;
OS   Ixodes ricinus (Common tick) (Acarus ricinus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=34613 {ECO:0000312|EMBL:JAC91915.1};
RN   [1] {ECO:0000312|EMBL:JAC91915.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=25970599; DOI=10.1371/journal.pntd.0003754;
RA   Kotsyfakis M., Kopacek P., Franta Z., Pedra J.H., Ribeiro J.M.;
RT   "Deep Sequencing Analysis of the Ixodes ricinus Haemocytome.";
RL   PLoS Negl. Trop. Dis. 9:e0003754-e0003754(2015).
RN   [2] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=31167786; DOI=10.1074/jbc.ra119.008817;
RA   Lee A.W., Deruaz M., Lynch C., Davies G., Singh K., Alenazi Y.,
RA   Eaton J.R.O., Kawamura A., Shaw J., Proudfoot A.E.I., Dias J.M.,
RA   Bhattacharya S.;
RT   "A knottin scaffold directs the CXC-chemokine-binding specificity of tick
RT   evasins.";
RL   J. Biol. Chem. 294:11199-11212(2019).
CC   -!- FUNCTION: Salivary chemokine-binding protein which binds to host
CC       chemokines CXCL1, CXCL2, CXCL3, CXCL5, CXCL6, CXCL12 and CXCL13.
CC       {ECO:0000269|PubMed:31167786}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR   EMBL; GBIH01002795; JAC91915.1; -; mRNA.
DR   AlphaFoldDB; A0A090XA85; -.
DR   SMR; A0A090XA85; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019958; F:C-X-C chemokine binding; IDA:UniProtKB.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..94
FT                   /note="Evasin P1104"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5001867002"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        48..66
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E8"
FT   DISULFID        52..68
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E8"
FT   DISULFID        62..79
FT                   /evidence="ECO:0000250|UniProtKB:P0C8E8"
SQ   SEQUENCE   94 AA;  9856 MW;  9169D0233A8CCA10 CRC64;
     MASNLFTIFQ LAGFVAIVFI VNLHSVSAES KEASASQGPG KSFKVEFCET NCTENNGVWS
     GCTGDCICVS VGDSKEGRCM DLGDKVIDTP VAQG